Dihydropteroate synthase
Details
- Name
- Dihydropteroate synthase
- Kind
- protein
- Synonyms
- 2.5.1.15
- DHPS
- Dihydropteroate pyrophosphorylase
- Gene Name
- folP1
- UniProtKB Entry
- P9WND1Swiss-Prot
- Organism
- Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
- NCBI Taxonomy ID
- 83332
- Amino acid sequence
>lcl|BSEQ0051132|Dihydropteroate synthase MSPAPVQVMGVLNVTDDSFSDGGCYLDLDDAVKHGLAMAAAGAGIVDVGGESSRPGATRV DPAVETSRVIPVVKELAAQGITVSIDTMRADVARAALQNGAQMVNDVSGGRADPAMGPLL AEADVPWVLMHWRAVSADTPHVPVRYGNVVAEVRADLLASVADAVAAGVDPARLVLDPGL GFAKTAQHNWAILHALPELVATGIPVLVGASRKRFLGALLAGPDGVMRPTDGRDTATAVI SALAALHGAWGVRVHDVRASVDAIKVVEAWMGAERIERDG
- Number of residues
- 280
- Molecular Weight
- 28842.685
- Theoretical pI
- Not Available
- GO Classification
- Functionsdihydropteroate synthase activity / metal ion bindingProcessesfolic acid biosynthetic process / growth / tetrahydrofolate biosynthetic processComponentscytosol
- General Function
- Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives.
- Specific Function
- dihydropteroate synthase activity
- Pfam Domain Function
- Pterin_bind (PF00809)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0051133|Dihydropteroate synthase (folP1) GTGAGTCCGGCGCCCGTGCAGGTGATGGGGGTTCTAAACGTCACGGACGACTCTTTCTCG GACGGCGGGTGTTATCTCGATCTCGACGATGCGGTGAAGCACGGTCTGGCGATGGCAGCC GCAGGTGCGGGCATCGTCGACGTCGGTGGTGAGTCGAGCCGGCCCGGTGCCACTCGGGTT GACCCGGCGGTGGAGACGTCTCGTGTCATACCCGTCGTCAAAGAGCTTGCAGCACAAGGC ATCACCGTCAGCATCGATACCATGCGCGCGGATGTCGCTCGGGCGGCGTTGCAGAACGGT GCCCAGATGGTCAACGACGTGTCGGGTGGGCGGGCCGATCCGGCGATGGGGCCGCTGTTG GCCGAGGCCGATGTGCCGTGGGTGTTGATGCACTGGCGGGCGGTATCGGCCGATACCCCG CATGTGCCTGTGCGCTACGGCAACGTGGTGGCCGAGGTCCGTGCCGACCTGCTGGCCAGC GTCGCCGACGCGGTGGCCGCAGGCGTCGACCCGGCAAGGCTGGTGCTCGATCCCGGGCTT GGATTCGCCAAGACGGCGCAACATAATTGGGCGATCTTGCATGCCCTTCCGGAACTGGTC GCGACCGGAATCCCAGTGCTGGTGGGTGCTTCGCGCAAGCGCTTCCTCGGTGCGTTGTTG GCCGGGCCCGACGGCGTGATGCGGCCAACCGATGGGCGTGACACCGCGACGGCGGTGATT TCCGCGCTGGCCGCACTGCACGGGGCCTGGGGTGTGCGGGTGCATGATGTGCGGGCCTCG GTCGATGCCATCAAGGTGGTCGAAGCGTGGATGGGAGCGGAAAGGATAGAACGCGATGGC TGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P9WND1 UniProtKB Entry Name DHPS1_MYCTU PDB ID(s) 1EYE KEGG ID mtu:Rv3608c NCBI Gene ID 885831 - General References
- Nopponpunth V, Sirawaraporn W, Greene PJ, Santi DV: Cloning and expression of Mycobacterium tuberculosis and Mycobacterium leprae dihydropteroate synthase in Escherichia coli. J Bacteriol. 1999 Nov;181(21):6814-21. [Article]
- Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [Article]
- Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3. [Article]
- Zheng J, Rubin EJ, Bifani P, Mathys V, Lim V, Au M, Jang J, Nam J, Dick T, Walker JR, Pethe K, Camacho LR: para-Aminosalicylic acid is a prodrug targeting dihydrofolate reductase in Mycobacterium tuberculosis. J Biol Chem. 2013 Aug 9;288(32):23447-56. doi: 10.1074/jbc.M113.475798. Epub 2013 Jun 18. [Article]
- Chakraborty S, Gruber T, Barry CE 3rd, Boshoff HI, Rhee KY: Para-aminosalicylic acid acts as an alternative substrate of folate metabolism in Mycobacterium tuberculosis. Science. 2013 Jan 4;339(6115):88-91. doi: 10.1126/science.1228980. Epub 2012 Nov 1. [Article]
- Baca AM, Sirawaraporn R, Turley S, Sirawaraporn W, Hol WG: Crystal structure of Mycobacterium tuberculosis 7,8-dihydropteroate synthase in complex with pterin monophosphate: new insight into the enzymatic mechanism and sulfa-drug action. J Mol Biol. 2000 Oct 6;302(5):1193-212. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Pterin-6-Yl-Methyl-Monophosphate experimental unknown target Details